ID SYR_BARBK Reviewed; 585 AA.
AC A1USU3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000255|HAMAP-Rule:MF_00123};
GN OrderedLocusNames=BARBAKC583_0749;
OS Bartonella bacilliformis (strain ATCC 35685 / KC583 / Herrer 020/F12,63).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=360095;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35685 / KC583 / Herrer 020/F12,63;
RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA Fraser-Ligget C., Seshadri R.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC EC=6.1.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR EMBL; CP000524; ABM44962.1; -; Genomic_DNA.
DR RefSeq; WP_005767024.1; NC_008783.1.
DR AlphaFoldDB; A1USU3; -.
DR SMR; A1USU3; -.
DR STRING; 360095.BARBAKC583_0749; -.
DR GeneID; 72472212; -.
DR KEGG; bbk:BARBAKC583_0749; -.
DR PATRIC; fig|360095.6.peg.727; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_5; -.
DR OrthoDB; 9803211at2; -.
DR Proteomes; UP000000643; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00671; ArgRS_core; 1.
DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00456; argS; 1.
DR PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM01016; Arg_tRNA_synt_N; 1.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..585
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000017989"
FT MOTIF 131..141
FT /note="'HIGH' region"
SQ SEQUENCE 585 AA; 66254 MW; 77937A5E538DC51B CRC64;
MNVFKNFEQK IKKSLKESDI KGKNGENLDL SKITVDPPRD SLHGDLSTNA SMVLAKSVGL
NPRTLAEKII ALLKDDPSID HLEVAGSGFI NIKLTKSFWH DVLKLMITSG TDYGRTQIGQ
GKQVNVEYVS ANPTGPMHVG HCRGAVVGDV LANLLQFAGY NVTKEYYIND AGKQIEILAA
SVLLRYREAL GETINKIPEG LYPGEYLIPL GQSLVQEFGD KLLTMDNEKA LSIVKERSID
AMMTMIRQDL ATLNIHHDVF FSERMLYMNN AQAIRNTIND LTLNGYVYKG KLSPPKGQTL
EDWEPHEQTL FRSTDVGDDQ DRVLIKSDGS YTYFAADVAY FRDKFHRHFD EMIYVLGADH
AGYVKRLEAV AKAISGNKAK LTAFLCQLVK LFRNGHPVRM SKREGSFITL RDVVKEVGRD
PVRFMMLYRK CEAPLDFDLE KVTEQSKDNP IFYVQYAHAR CHSVFRQAQE NLQIENPSND
LMIAHLDQLT NDSEISLIHK LAQYPRIIEQ AIVYKEPHRL AFYLYDLASN FHGHWNKGND
NPELRFIKPN NKKLSLARLG LVQAFINVLS SGLKIVEVKA PTEMR
//
